7LZI
Structure of the glutamate receptor-like channel AtGLR3.4
Summary for 7LZI
| Entry DOI | 10.2210/pdb7lzi/pdb |
| EMDB information | 23606 23607 |
| Descriptor | Glutamate receptor 3.4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLUTAMIC ACID (3 entities in total) |
| Functional Keywords | arabidopsis thaliana, ion-channel, glutamate receptor-like channel (glr), transport protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 4 |
| Total formula weight | 431555.65 |
| Authors | Gangwar, S.P.,Green, M.N.,Sobolevsky, A.I. (deposition date: 2021-03-09, release date: 2021-07-28, Last modification date: 2024-11-13) |
| Primary citation | Green, M.N.,Gangwar, S.P.,Michard, E.,Simon, A.A.,Portes, M.T.,Barbosa-Caro, J.,Wudick, M.M.,Lizzio, M.A.,Klykov, O.,Yelshanskaya, M.V.,Feijo, J.A.,Sobolevsky, A.I. Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol.Cell, 81:3216-, 2021 Cited by PubMed Abstract: Glutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their molecular organization is limited. Here we use X-ray crystallography and single-particle cryo-EM to solve structures of the Arabidopsis thaliana GLR3.4. Our structures reveal the tetrameric assembly of GLR3.4 subunits into a three-layer domain architecture, reminiscent of animal ionotropic glutamate receptors (iGluRs). However, the non-swapped arrangement between layers of GLR3.4 domains, binding of glutathione through S-glutathionylation of cysteine C205 inside the amino-terminal domain clamshell, unique symmetry, inter-domain interfaces, and ligand specificity distinguish GLR3.4 from representatives of the iGluR family and suggest distinct features of the GLR gating mechanism. Our work elaborates on the principles of GLR architecture and symmetry and provides a molecular template for deciphering GLR-dependent signaling mechanisms in plants. PubMed: 34161757DOI: 10.1016/j.molcel.2021.05.025 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.39 Å) |
Structure validation
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